Membrane Tubulina

Regula, C S; Sager, Polly R.; Berlin, Richard D.

doi:10.1111/j.1749-6632.1986.tb38466.x

Cited by 15 publications

(7 citation statements)

References 21 publications

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“…Membrane-or phospholipid-associated tubulin has been reported (Bhattacharyya and Wolff, 1976;Klausner et al, 1981;Kumar et al, 1981;Reaven and Azhar, 1981;Regula et al, 1986;Caron and Berlin, 1987). It appeared that this "membrane" tubulin was similar to the soluble form (Bhattacharyya and Wolff, 1976;Stephens, 1977).…”

Section: Discussionmentioning

confidence: 82%

Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ₁Signaling

Popova¹,

Greene²,

Wang³

et al. 2002

J. Neurosci.

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Section: Discussionmentioning

confidence: 82%

Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ₁Signaling

Popova¹,

Greene²,

Wang³

et al. 2002

J. Neurosci.

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“…Tubulin and other membrane proteins were extracted sequentially from synaptic membranes as described (Regula et al, 1986). Cerebral cortex membranes were stirred on ice in 1% Triton X-100 in HEPES (15 mM, pH 7.4) for 60 mm followed by centrifugation at 100,000 g for 60 mm at 4°C.…”

Section: Membrane Tubulin Extractionmentioning

confidence: 99%

“…Two populations of membrane tubulin that have distinct hydrophobicities have been postulated (Regula et al, 1986). These two populations of tubulin can be extracted by two different strength detergents: Triton X-lOO and Triton X-l 14.…”

Section: Tubulin-g Protein Complexes In the Synaptic Membranementioning

confidence: 99%

Synaptic Membrane G Proteins Are Complexed with Tubulin In Situ

Kou

Greene²,

Belga³

et al. 1996

Journal of Neurochemistry

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The G proteins G 5 and G~1appear to be capable of binding to tubulin specifically, and it has been suggested that such binding results in G protein activation via direct transfer of GTP. This study was undertaken to demonstrate that consequences of G protein activation by tubulin, i.e., stimulation or inhibition of adenylyl cyclase, were dependent on the G proteins expressed as well as unique aspects of the membrane or cytoskeleton in a given cell type. Membranes from rat 06 glioma cells, which express G5,, but not G~,,1, responded to the addition of tubulin with a stable activation of adenylyl cyclase. Conversely, membranes from rat cerebral cortex, which contain both G5 and G1, responded to exogenous tubulin with a stable inhibition of adenylyl cyclase. Unlike 06 membranes, cerebral cortex membranes are richly endowed with tubulin, and antitubulin antibodies immuno-precipi~atedcomplexes of tubulin and G,1 or G5 from detergent extracts of these membranes. Nearly 90% of the G5,, from Triton X-114 extracts coimmunoprecipitated with tubu~n,suggesting that these proteins exist as a complex in the synaptic membrane. Such complexes may provide the framework for a G protein-cytoskeleton link that participates in the modulation of cellular signal transduction.

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“…However, microtubule is a cytosolic structure protein, and PLD 2 a membrane-bound protein. Although, membrane-and phospholipid-associated tubulin have been reported (55)(56)(57), it appears that this membrane tubulin is similar to the monomeric form (55,57,59). This notion is supported by observations of the COS-7 cells treated with the microtubule stability regulating pharmacological agents nocodazole and Taxol.…”

Section: Figmentioning

confidence: 99%

Inhibition of Muscarinic Receptor-linked Phospholipase D Activation by Association with Tubulin

Chae

Lee

et al. 2005

Journal of Biological Chemistry

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Mammalian phospholipase D (PLD) is considered a key enzyme in the transmission signals from various receptors including muscarinic receptors. PLD activation is a rapid and transient process, but a negative regulator has not been found that inhibits signal-dependent PLD activation. Here, for the first time, we report that tubulin binding to PLD 2 is an inhibition mechanism for muscarinic receptor-linked PLD 2 activation. Tubulin was identified in an immunoprecipitated PLD 2 complex from COS-7 cells by peptide mass fingerprinting. The direct interaction between PLD 2 and tubulin was found to be mediated by a specific region of PLD 2 (amino acids 476 -612). PLD 2 was potently inhibited (IC 50 <10 nM) by tubulin binding in vitro. In cells, the interaction between PLD 2 and tubulin was increased by the microtubule disrupting agent nocodazole and reduced by the microtubule stabilizing agent Taxol. Moreover, PLD 2 activity was found to be inversely correlated with the level of monomeric tubulin. In addition, we found that interaction with and the inhibition of PLD 2 by monomeric tubulin is important for the muscarinic receptor-linked PLD signaling pathway. Interaction between PLD 2 and tubulin was increased only after 1-2 min of carbachol stimulation when carbachol-stimulated PLD 2 activity was decreased. The expression of the tubulin binding region of PLD 2 blocked the later decrease in carbachol-induced PLD activity by masking tubulin binding. Taken together, these results indicate that an increase in local membrane monomeric tubulin concentration inhibits PLD 2 activity, and provides a novel mechanism for the inhibition of muscarinic receptor-induced PLD 2 activation by interaction with tubulin. Mammalian phospholipase D (PLD)1 hydrolyzes membrane phosphatidylcholine to generate phosphatidic acid and choline. PLD activity is dramatically activated in response to a variety of signals, including hormones, neurotransmitters, and growth factors (1). PLD products, phosphatidic acid itself or the hydrolyzed product diacylglycerol, have been known to act as intracellular lipid second messengers and to be involved in multiple physiological events, such as, the promotion of mitogenesis, stimulation of respiratory bursts, secretory processes, and actin cytoskeletal reorganization (2-7). Therefore, signal-dependent PLD activity must be tightly controlled in cells.Many reports have been issued about the mechanisms of receptor-mediated PLD activation. Although the mammalian PLD isozymes, PLD 1 and PLD 2 , have some different regulatory properties, in general, agonist-induced PLD is activated by various protein kinases, including protein kinase C, proteintyrosine kinase, and the MAP kinase family, in addition to small G proteins of the ARF, Rho, and Ras families (8 -13). The signal-dependent activation of PLD is rapid and transient. Although, the activation kinetics depend on the stimulus and cell type, the PLD signal is usually diminished within 10 min (14). However, the mechanisms involved in PLD signal inhibition remain unknow...

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Membrane Tubulina

Cited by 15 publications

References 21 publications

Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ₁Signaling

Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ₁Signaling

Synaptic Membrane G Proteins Are Complexed with Tubulin In Situ

Inhibition of Muscarinic Receptor-linked Phospholipase D Activation by Association with Tubulin

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Membrane Tubulina

Cited by 15 publications

References 21 publications

Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ1Signaling

Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ1Signaling

Synaptic Membrane G Proteins Are Complexed with Tubulin In Situ

Inhibition of Muscarinic Receptor-linked Phospholipase D Activation by Association with Tubulin

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Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ₁Signaling

Phosphatidylinositol 4,5-Bisphosphate Modifies Tubulin Participation in Phospholipase Cβ₁Signaling